PERFORMANCE ANALYSIS OF AN ENERGY EFFICIENT FFT PROCESSOR USING 32nm CMOS TECHNOLOGY

ABSTRACT This paper presents an energy-efficient Fast Fourier Transform (FFT) processor which meets the requirements of DSP applications. Fast Fourier Transform is one of the widely used digital signals processing (DSP) algorithms which analysis the signal in its frequency domain. Modified DOMS-FF (Duration Observation Master Slave-Flip Flop) is introduced to reduce the power dissipation and makes the computation of the result much faster than the existing system. The goal of this work is to get less area and energy efficient FFT processor with build in all requirements necessary for DSP applications

GC-MS analysis of bioactive compounds from Freshwater mussels of Parreysia corrugata (Muller 1774) and their pharmacological activities

GC-MS is one of the best techniques to identify the constituents of volatile matter, long chain, branched chain hydrocarbons, alcohols acids, esters etc. The freshwater mussels Parreysia corrugata was analyzed using Gas Chromatography–Mass Spectrometry, while the mass spectra of the compounds found in the extract was matched with the National Institute of Standards and Technology (NIST) library. Gas chromatography mass spectrometry (GC-MS) analysis revealed the presence of 26 compounds. The compounds were identified by comparing their retention time and peak area with that of literature and by interpretation of mass spectra. The first compound identified with less retention time (30.236 min) was 2,6-Difluorobenzoic acid, tridec-2-ynyl ester, whereas gamma.-Tocopherol was the last compound which took longest retention time (29.84min) to identify. Many of them are used in industry for various applications like flavor, antioxidant, anti-inflammatory, antimicrobial, pesticide and cancer preventive. Keywords: Freshwater mussels, Parreysia corrugata, GC-MS, Bioactive component

INTERNATIONAL JOURNAL OF PHARMACY & LIFE SCIENCES Antibacterial activity of freshwater Mussel Parreysia corrugata (Muller 1774) from Lower Anaicut Reservoir, India

Abstract In the present study aqueous, ethanol and methanol extracts of freshwater mussel Parreysia corrugata were screened for antibacterial activity. The extracts were obtained from the whole body tissue of the animals and tested against 5 pathogenic bacteria viz., Klebsiella pneumoniae, Pseudomonas aeruginosa, Salmonella typhi, Enterococcus faecalis and Staphylococcus aureus. Ethanol extract of P.corrugata showed maximum antibacterial activity 11 mm against P.aeruginosa and the minimum activity 9 mm against K. pneumoniae. Methanol extract of P.corrugata showed Maximum inhibition 13mm against P.aeruginosa and the minimum inhibition zone of 8mm against K. pneumoniae. Aqueous extract of P.corrugata showed the maximum inhibition zone was 10mm against S.aureus and the minimum inhibition zone was 7 mm against S.typhi. Aqueous, Ethanol and Methanol extracts showed antibacterial activity against five human pathogen bacteria tested. Compare to water extracts Ethanol and Methanol extracts showed more activity against all pathogens. FTIR analysis revealed the presence of bioactive compounds signals at different ranges

(1S,1′S,2′R,4a'S,9a'S,9b'R)-1′-Acetyloxy-2,4′-dioxo-2′,4′,4a',7′,8′,9′,9a',9b'-octahydro-1′H,2H-spiro[acenaphthylene-1,5′-pyrano[4,3-a]pyrrolizin]-2′-ylmethyl acetate

In the title compound C26H25NO7, the mean plane through the lactone-substituted ring of the pyrrolizidine moiety forms dihedral angles of 78.46 (6) and 58.28 (8)° with the acenaphthylene moiety and the sugar based-lactone ring, respectively. The sum of the angles at the the N atom of the pyrrolizidine ring (335.0°) is in accordance with sp3 hybridization. Some atoms of the acetate group are disordered and were refined using a split model [occupancy ratio 0.673 (10):0.327 (10)]

Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family.

Purpose: The aim of the present study was to investigate the molecular basis underlying a nonsyndromic presenile autosomal dominant cataract in a three-generation pedigree. The phenotype was progressive from a peripheral ring-like opacity to a total cataract with advancing age from teenage to adulthood. The visual impairment started as problem in distant vision at the age of 16 years, to diminishing vision by the age of 24. Methods: Clinical interventions included complete ophthalmological examination, a collection of case history, and pedigree details. Blood samples were collected from available family members irrespective of their clinical status. A functional candidate gene approach was employed for PCR screening and sequencing of the exons and their flanking regions of CRYGC, CRYGD, and CRYAA genes. For structural consequences of the mutated alpha A-crystallin we used the bioinformatics tool of the ExPASy server. Results: Sequence analysis of CRYGC and CRYGD genes excluded possible causative mutations but identified known polymorphisms. Sequencing of the exons of the CRYAA gene identified a sequence variation in exon 2 (292 G-> A) with a substitution of Gly to Arg at position 98. All three affected members revealed this change but it was not observed in the unaffected father or sister. The putative mutation obliterated a restriction site for the enzyme BstDSI. The same was checked in controls representing the general population of the same ethnicity (n=30) and of randomly selected DNA samples from ophthalmologically normal individuals from the population-based KORA S4 study (n=96). Moreover, the Gly at position 98 is highly conserved throughout the animal kingdom. For the mutant protein, the isoelectric point was raised from pH 5.77 to 5.96. Moreover, an extended alpha-helical structure is predicted in this region. Conclusions: The G98R mutation segregates only in affected family members and is not seen in representative controls. It represents very likely the fourth dominant cataract-causing allele in CRYAA. In all reported alleles the basic amino acid Arg is involved, suggesting the major importance of the net charge of the alpha A-crystallin for functional integrity in the lens

Molecular analysis of cataract families in India: New mutations in the <em>CRYBB2</em> and <em>GJA3</em> genes and rare polymorphisms.

PURPOSE: The aim of the study was to resolve the genetic etiology in families having inherited cataracts. METHODS: Families afflicted with congenital/childhood cataracts were registered in Chennai and Orissa (India). Blood samples were collected from the probands and available family members. Selected functional candidate genes were amplified by polymerase chain reaction (PCR) and characterized by direct sequencing. Putative mutations were confirmed in healthy controls. RESULTS: We observed interesting new polymorphisms of ethnic specificity, some of frequent nature, such as a 3-bp deletion in intron 3 of CRYBB2 (encoding &beta;B2-crystallin) and IVS1+9 c&gt;t variation in HSF4 (encoding heat-shock factor 4). Some rare single nucleotide polymorphisms (SNPs) co-segregate with the respective phenotype such as IVS3+120c&gt;a of CRYBB2, while M44V of CRYGD (encoding &gamma;D-crystallin), although found in association with blue dot opacity was seen in a few healthy controls too. We identified two new mutations co-segregating along with the respective cataract phenotype within the families that were not seen in healthy controls from India or Germany. These include two missense mutations; one in GJA3 (encoding gap junction protein &alpha;3, which is also referred to as connexin 46); the mutation affects codon 19 (T19M), and the corresponding phenotype is a posterior-polar cataract. The other missense mutation affects CRYBB2 (W59C; total cataract). Additionally, a cDNA variation (G54A) identified in a zonular cataract affects a highly conserved splice site of CRYBB2. This mutation, however, showed reduced penetrance in the family, which might be explained by different molecular consequences in the affected family members: nonsense-mediated decay of the mutated mRNA might have no clinical phenotype in heterozygotes, whereas the translation of the mutated mRNA is predicted to lead to a small hybrid protein (consisting of 16 amino acids of the &beta;B2-crystallin and 18 new amino-acids), which might have a dominant-negative function in the lens. CONCLUSIONS: This report identifies in families with childhood cataract some new alleles, which may be considered as causative for cataracts. Furthermore, we report some geographically restricted rare polymorphic sites, whose significance might be considered in some context as modifiers or alleles in sensitizing ocular lens toward cataractogenesis